ENPL_HUMAN
ID ENPL_HUMAN Reviewed; 803 AA.
AC P14625; Q96A97;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 245.
DE RecName: Full=Endoplasmin;
DE AltName: Full=94 kDa glucose-regulated protein;
DE Short=GRP-94;
DE AltName: Full=Heat shock protein 90 kDa beta member 1;
DE AltName: Full=Tumor rejection antigen 1;
DE AltName: Full=gp96 homolog;
DE Flags: Precursor;
GN Name=HSP90B1 {ECO:0000312|HGNC:HGNC:12028}; Synonyms=GRP94, TRA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RC TISSUE=Blood;
RX PubMed=2377606; DOI=10.1073/pnas.87.15.5658;
RA Maki R.G., Old L.J., Srivastava P.K.;
RT "Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and
RT coding regions and relationship to stress-induced proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5658-5662(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RC TISSUE=Liver;
RX PubMed=2546060; DOI=10.1128/mcb.9.5.2153-2162.1989;
RA Chang S.C., Erwin A.E., Lee A.S.;
RT "Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory
RT domains and are coordinately regulated by common trans-acting factors.";
RL Mol. Cell. Biol. 9:2153-2162(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-803.
RC TISSUE=Liver;
RA Meng S., Tien P.;
RT "The association of heat shock protein gp96 with HBV-derived peptides in
RT vitro.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 22-39.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP COMPONENT OF A CHAPERONE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [8]
RP GLYCOSYLATION AT ASN-217 AND ASN-445.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP INTERACTION WITH CNPY3; TLR4 AND TLR9.
RX PubMed=20865800; DOI=10.1038/ncomms1070;
RA Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B.,
RA Bona R., Han D., Li Z.;
RT "Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a
RT substrate-specific cochaperone.";
RL Nat. Commun. 1:79-79(2010).
RN [11]
RP ERRATUM OF PUBMED:20865800.
RA Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B.,
RA Bona R., Han D., Li Z.;
RL Nat. Commun. 3:653-653(2012).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [14]
RP FUNCTION, AND INTERACTION WITH OS9.
RX PubMed=18264092; DOI=10.1038/ncb1689;
RA Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.;
RT "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L
RT ubiquitin ligase complex for ERAD.";
RL Nat. Cell Biol. 10:272-282(2008).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-107; ASN-217 AND
RP ASN-445.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP INTERACTION WITH METTL23.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-447 AND THR-786, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP PHOSPHORYLATION AT SER-306.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [23]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-21, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP HYDROXYBUTYRYLATION AT LYS-168.
RX PubMed=29192674; DOI=10.1038/cr.2017.149;
RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT pathway.";
RL Cell Res. 28:111-125(2018).
RN [25]
RP FUNCTION, AND INTERACTION WITH IL1B.
RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031;
RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X.,
RA Zhang D., Lv X., Zheng L., Ge L.;
RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein
RT Secretion.";
RL Cell 181:637-652(2020).
CC -!- FUNCTION: Molecular chaperone that functions in the processing and
CC transport of secreted proteins (By similarity). When associated with
CC CNPY3, required for proper folding of Toll-like receptors (By
CC similarity). Functions in endoplasmic reticulum associated degradation
CC (ERAD) (PubMed:18264092). Has ATPase activity (By similarity). May
CC participate in the unfolding of cytosolic leaderless cargos (lacking
CC the secretion signal sequence) such as the interleukin 1/IL-1 to
CC facilitate their translocation into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) and secretion; the translocation
CC process is mediated by the cargo receptor TMED10 (PubMed:32272059).
CC {ECO:0000250|UniProtKB:P08113, ECO:0000269|PubMed:18264092,
CC ECO:0000269|PubMed:32272059}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex at
CC least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1
CC and HSPA5 (By similarity). Part of a large chaperone multiprotein
CC complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6,
CC PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at
CC very low levels, CALR nor CANX. Interacts with AIMP1; regulates its
CC retention in the endoplasmic reticulum. Interacts with OS9. Interacts
CC with CNPY3. This interaction is disrupted in the presence of ATP (By
CC similarity). Interacts with TLR4 and TLR9, but not with TLR3. Interacts
CC with MZB1 in a calcium-dependent manner (By similarity). Interacts with
CC METTL23. Interacts with IL1B; the interaction facilitates cargo
CC translocation into the ERGIC (PubMed:32272059). {ECO:0000250,
CC ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:20865800,
CC ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:32272059}.
CC -!- INTERACTION:
CC P14625; P05067: APP; NbExp=3; IntAct=EBI-359129, EBI-77613;
CC P14625; P04626: ERBB2; NbExp=2; IntAct=EBI-359129, EBI-641062;
CC P14625; Q00597: FANCC; NbExp=4; IntAct=EBI-359129, EBI-81625;
CC P14625; P11021: HSPA5; NbExp=2; IntAct=EBI-359129, EBI-354921;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000305|PubMed:12475965}. Sarcoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P41148}. Melanosome
CC {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}.
CC Note=Identified by mass spectrometry in melanosome fractions from stage
CC I to stage IV. {ECO:0000269|PubMed:12643545,
CC ECO:0000269|PubMed:17081065}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; X15187; CAA33261.1; -; mRNA.
DR EMBL; M33716; AAA68201.1; -; Genomic_DNA.
DR EMBL; BC066656; AAH66656.1; -; mRNA.
DR EMBL; M26596; AAA58621.1; -; Genomic_DNA.
DR EMBL; AY040226; AAK74072.1; -; mRNA.
DR CCDS; CCDS9094.1; -.
DR PIR; A35954; A35954.
DR RefSeq; NP_003290.1; NM_003299.2.
DR PDB; 4NH9; X-ray; 2.77 A; A=69-337.
DR PDBsum; 4NH9; -.
DR AlphaFoldDB; P14625; -.
DR SMR; P14625; -.
DR BioGRID; 113036; 462.
DR CORUM; P14625; -.
DR DIP; DIP-36060N; -.
DR IntAct; P14625; 190.
DR MINT; P14625; -.
DR STRING; 9606.ENSP00000299767; -.
DR BindingDB; P14625; -.
DR ChEMBL; CHEMBL1075323; -.
DR DrugBank; DB08465; 2-(3-AMINO-2,5,6-TRIMETHOXYPHENYL)ETHYL 5-CHLORO-2,4-DIHYDROXYBENZOATE.
DR DrugBank; DB02103; 2-Chlorodideoxyadenosine.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB02935; Diglyme.
DR DrugBank; DB02424; Geldanamycin.
DR DrugBank; DB08464; METHYL 3-CHLORO-2-{3-[(2,5-DIHYDROXY-4-METHOXYPHENYL)AMINO]-3-OXOPROPYL}-4,6-DIHYDROXYBENZOATE.
DR DrugBank; DB03719; N-Ethyl-5'-Carboxamido Adenosine.
DR DrugBank; DB03758; Radicicol.
DR DrugBank; DB00615; Rifabutin.
DR GuidetoPHARMACOLOGY; 2904; -.
DR GlyConnect; 1206; 15 N-Linked glycans (5 sites).
DR GlyGen; P14625; 11 sites, 19 N-linked glycans (5 sites), 1 O-linked glycan (3 sites).
DR iPTMnet; P14625; -.
DR MetOSite; P14625; -.
DR PhosphoSitePlus; P14625; -.
DR SwissPalm; P14625; -.
DR BioMuta; HSP90B1; -.
DR DMDM; 119360; -.
DR DOSAC-COBS-2DPAGE; P14625; -.
DR OGP; P14625; -.
DR REPRODUCTION-2DPAGE; IPI00027230; -.
DR CPTAC; CPTAC-1278; -.
DR CPTAC; CPTAC-1279; -.
DR EPD; P14625; -.
DR jPOST; P14625; -.
DR MassIVE; P14625; -.
DR PaxDb; P14625; -.
DR PeptideAtlas; P14625; -.
DR PRIDE; P14625; -.
DR ProteomicsDB; 53067; -.
DR TopDownProteomics; P14625; -.
DR ABCD; P14625; 4 sequenced antibodies.
DR Antibodypedia; 1290; 1381 antibodies from 49 providers.
DR DNASU; 7184; -.
DR Ensembl; ENST00000299767.10; ENSP00000299767.4; ENSG00000166598.16.
DR GeneID; 7184; -.
DR KEGG; hsa:7184; -.
DR MANE-Select; ENST00000299767.10; ENSP00000299767.4; NM_003299.3; NP_003290.1.
DR CTD; 7184; -.
DR DisGeNET; 7184; -.
DR GeneCards; HSP90B1; -.
DR HGNC; HGNC:12028; HSP90B1.
DR HPA; ENSG00000166598; Low tissue specificity.
DR MIM; 191175; gene.
DR neXtProt; NX_P14625; -.
DR OpenTargets; ENSG00000166598; -.
DR PharmGKB; PA36705; -.
DR VEuPathDB; HostDB:ENSG00000166598; -.
DR eggNOG; KOG0020; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P14625; -.
DR OMA; KVSKTTW; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P14625; -.
DR TreeFam; TF105969; -.
DR PathwayCommons; P14625; -.
DR Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P14625; -.
DR SIGNOR; P14625; -.
DR BioGRID-ORCS; 7184; 402 hits in 1091 CRISPR screens.
DR ChiTaRS; HSP90B1; human.
DR GeneWiki; HSP90B1; -.
DR GenomeRNAi; 7184; -.
DR Pharos; P14625; Tchem.
DR PRO; PR:P14625; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P14625; protein.
DR Bgee; ENSG00000166598; Expressed in right lobe of thyroid gland and 210 other tissues.
DR ExpressionAtlas; P14625; baseline and differential.
DR Genevisible; P14625; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0097524; C:sperm plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0031247; P:actin rod assembly; IDA:MGI.
DR GO; GO:0071318; P:cellular response to ATP; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051208; P:sequestering of calcium ion; NAS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Calcium; Chaperone;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydroxylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 22..803
FT /note="Endoplasmin"
FT /id="PRO_0000013598"
FT REGION 288..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 800..803
FT /note="Prevents secretion from ER"
FT COMPBIAS 290..314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..790
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT SITE 448
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 168
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29192674"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT MOD_RES 306
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT MOD_RES 404
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 479
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 633
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 786
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 138
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 188
FT /note="T -> S (in Ref. 4; AAK74072)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="T -> P (in Ref. 4; AAK74072)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="L -> F (in Ref. 4; AAK74072)"
FT /evidence="ECO:0000305"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:4NH9"
FT HELIX 99..118
FT /evidence="ECO:0007829|PDB:4NH9"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:4NH9"
FT TURN 123..128
FT /evidence="ECO:0007829|PDB:4NH9"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4NH9"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:4NH9"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4NH9"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:4NH9"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:4NH9"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:4NH9"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:4NH9"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:4NH9"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:4NH9"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:4NH9"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:4NH9"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:4NH9"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:4NH9"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:4NH9"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:4NH9"
SQ SEQUENCE 803 AA; 92469 MW; 9BF6705A7A2ED0D0 CRC64;
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL
TDENALSGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE
AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT
LGRGTTITLV LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADDKY
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHPTD ITSLDQYVER MKEKQDKIYF
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
SEKTKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR IKEDEDDKTV LDLAVVLFET
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PDAKVEEEPE EEPEETAEDT TEDTEQDEDE
EMDVGTDEEE ETAKESTAEK DEL
